Abstract

Continuous enzymatic reaction has been proven as an efficient technique for several industrial applications. In
this study, a type of hollow fiber membrane bioreactor where penicillin acylase entrapped within membrane pores
was applied to continuously hydrolyze Penicillin G The influences of various operating conditions on immobilization
and enzymatic reaction processes were assessed. Amathematical model of the reactor behaviour at steady state condition
was also developed. The immobilization results show that penicillin acylase was entrapped more than 90%
(100,000 u.a m-?). Due to the much smaller size of 6-APA compared to the membrane pore, the solute diffuses freely
through the membrane. However, the immobilized enzyme membrane retained around 35% of the solute. In addition,
K,,, of immobilized penicillin acylase (8.04 mM) was slightly higher than that of free penicillin acylase (7.75 mM).
The theoretical results indicated that convective transport was the main mechanism of mass transport even in the
case where flux was very low. Low flux rate is important to avoid gel formation or enzyme release from membrane
pores and to maximize the degree of conversion.